The analgesic activity of some kyotorphin-tuftsin analogs.
The analgesic potency of the C-terminal dipeptide of tuftsin (Pro-Arg) was found to be much stronger than that of the C-terminal of bradykinin dipeptide Phe-Arg. It was also found that the tripeptide fragment of bradykinin (Pro-Phe-Arg) and its D-Pro analog (D-Pro-Phe-Arg) are deprived of analgesic activity. The attempt to synthesize kyotorphin analogs containing fluorescence label (DMAPhe-Arg and D-DMAPhe-Arg; DMAPhe: 4'-dimethylamino-phenylalanine) resulted in inactive compounds.
Siemion
I Z
IZ
Institute of Chemistry, Wrocław University, Poland.
Kubik
A
A
Nawrocka
E
E
Obuchowicz
E
E
Gołba
K
K
Herman
Z S
ZS
D000595:Amino Acid Sequence; D000818:Animals; D004151:Dipeptides / Q000138:chemical synthesis / Q000494:pharmacology; D004723:Endorphins / Q000494:pharmacology*; D005453:Fluorescence; D008297:Male; D008969:Molecular Sequence Data; D010147:Pain Measurement / Q000187:drug effects; D010455:Peptides / Q000138:chemical synthesis / Q000494:pharmacology; D010649:Phenylalanine / Q000031:analogs & derivatives / Q000494:pharmacology; D051381:Rats; D011919:Rats, Inbred Strains; D014405:Tuftsin / Q000494:pharmacology*
D004151:Dipeptides; D004723:Endorphins; D010455:Peptides; C019448:kyotorphin; C067005:4'-dimethylaminophenylalanine; D010649:Phenylalanine; D014405:Tuftsin